Structure of PDB 4nir Chain A

Receptor sequence
>4nirA (length=274) Species: 1392 (Bacillus anthracis) [Search protein sequence]
MKWDYDLRCGEYTLNLNEKTLIMGILNVTPDSFSDGGSYNEVDAAVRHAK
EMRDEGAHIIDIGGESTRPGFAKVSVEEEIKRVVPMIQAVSKEVKLPISI
DTYKAEVAKQAIEAGAHIINDIWGAKAEPKIAEVAAHYDVPIILMHNRDN
MNYRNLMADMIADLYDSIKIAKDAGVRDENIILDPGIGFAKTPEQNLEAM
RNLEQLNVLGYPVLLGTSRKSFIGHVLDLPVEERLEGTGATVCLGIEKGC
EFVRVHDVKEMSRMAKMMDAMIGK
3D structure
PDB4nir Identification and characterization of an allosteric inhibitory site on dihydropteroate synthase.
ChainA
Resolution1.772 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) V28 D54 K220 R254
Catalytic site (residue number reindexed from 1) V28 D54 K220 R254
Enzyme Commision number 2.5.1.15: dihydropteroate synthase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 6DH A W123 R148 D149 W123 R148 D149
BS02 6DH A L235 E236 E260 L235 E236 E260
Gene Ontology
Molecular Function
GO:0004156 dihydropteroate synthase activity
GO:0016740 transferase activity
GO:0046872 metal ion binding
Biological Process
GO:0009396 folic acid-containing compound biosynthetic process
GO:0042558 pteridine-containing compound metabolic process
GO:0044237 cellular metabolic process
GO:0046654 tetrahydrofolate biosynthetic process
GO:0046656 folic acid biosynthetic process
Cellular Component
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:4nir, PDBe:4nir, PDBj:4nir
PDBsum4nir
PubMed24650357
UniProtQ81VW8

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